dbPTM

HBAZ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HBAZ_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	P02008
Protein Name	Hemoglobin subunit zeta
Gene Name	HBZ
Organism	Homo sapiens (Human).
Sequence Length	142
Subcellular Localization
Protein Description	The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin..
Protein Sequence	MSLTKTERTIIVSMWAKISTQADTIGTETLERLFLSHPQTKTYFPHFDLHPGSAQLRAHGSKVVAAVGDAVKSIDDIGGALSKLSELHAYILRVDPVNFKLLSHCLLVTLAARFPADFTAEAHAAWDKFLSVVSSVLTEKYR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLTKTERT ------CCCCCCCHH	44.75	19664994
2	Acetylation	------MSLTKTERT ------CCCCCCCHH	44.75	19664994
4	Phosphorylation	----MSLTKTERTII ----CCCCCCCHHEE	28.72	24719451
5	Acetylation	---MSLTKTERTIIV ---CCCCCCCHHEEE	54.40	7960869
6	Phosphorylation	--MSLTKTERTIIVS --CCCCCCCHHEEEE	26.01	27251275
19	Phosphorylation	VSMWAKISTQADTIG EEEHHHHHCCCCCCC	17.48	23186163
20	Phosphorylation	SMWAKISTQADTIGT EEHHHHHCCCCCCCH	31.11	23186163
24	Phosphorylation	KISTQADTIGTETLE HHHCCCCCCCHHHHH	25.07	23186163
29	Phosphorylation	ADTIGTETLERLFLS CCCCCHHHHHHHHHH	33.48	23917254
36	Phosphorylation	TLERLFLSHPQTKTY HHHHHHHHCCCCCCC	26.28	23186163
40	Phosphorylation	LFLSHPQTKTYFPHF HHHHCCCCCCCCCCC	29.79	23917254
41	Acetylation	FLSHPQTKTYFPHFD HHHCCCCCCCCCCCC	35.66	7395805
41	Ubiquitination	FLSHPQTKTYFPHFD HHHCCCCCCCCCCCC	35.66	-
42	Phosphorylation	LSHPQTKTYFPHFDL HHCCCCCCCCCCCCC	33.51	23186163
43	Phosphorylation	SHPQTKTYFPHFDLH HCCCCCCCCCCCCCC	19.37	23186163
53	Phosphorylation	HFDLHPGSAQLRAHG CCCCCCCCHHHHHCC	19.79	23917254
62	Ubiquitination	QLRAHGSKVVAAVGD HHHHCCCEEEEEHHH	45.37	-
73	Phosphorylation	AVGDAVKSIDDIGGA EHHHHHHCHHHHHHH	25.34	23186163
82	Phosphorylation	DDIGGALSKLSELHA HHHHHHHHHHHHHHH	30.89	23917254
83	Ubiquitination	DIGGALSKLSELHAY HHHHHHHHHHHHHHH	57.81	-
83	Acetylation	DIGGALSKLSELHAY HHHHHHHHHHHHHHH	57.81	30585647
90	Phosphorylation	KLSELHAYILRVDPV HHHHHHHHHHCCCCC	6.96	23917254
100	Acetylation	RVDPVNFKLLSHCLL CCCCCCHHHHHHHHH	43.23	7665091
131	Phosphorylation	AAWDKFLSVVSSVLT HHHHHHHHHHHHHHH	24.49	23898821
134	Phosphorylation	DKFLSVVSSVLTEKY HHHHHHHHHHHHHHC	16.75	23898821
135	Phosphorylation	KFLSVVSSVLTEKYR HHHHHHHHHHHHHCC	14.99	23898821
138	Phosphorylation	SVVSSVLTEKYR--- HHHHHHHHHHCC---	28.42	23898821

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of HBAZ_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HBAZ_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HBAZ_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SP1_HUMAN	SP1	physical	18078517
JUND_HUMAN	JUND	physical	18078517
A4_HUMAN	APP	physical	21832049
DOCK8_HUMAN	DOCK8	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KHDR2_HUMAN	KHDRBS2	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
SIR5_HUMAN	SIRT5	physical	28514442
MY18A_HUMAN	MYO18A	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HBAZ_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"The role of beta chains in the control of the hemoglobin oxygenbinding function: chimeric human/mouse proteins, structure, andfunction."; Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.; Biochemistry 40:15669-15675(2001). Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-141 IN COMPLEX WITH MOUSEHBB, REMOVAL OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2.	11747442 [Abstract]
"Human embryonic haemoglobins. Ac-Ser-Leu-Thr-is the N-terminalsequence of the zeta-chains."; Aschauer H., Schaefer W., Sanguansermsri T., Braunitzer G.; Hoppe-Seyler's Z. Physiol. Chem. 362:1657-1659(1981). Cited for: ACETYLATION AT SER-2.	6172357 [Abstract]